Disease relevance of C01888

• The wild strain of Serratia marcescens rapidly degraded threonine and formed aminoacetone in a medium containing glucose and urea [1].
• The catalytic activity of this enzyme is elevated in diabetes mellitus and some substrates, such as aminoacetone and methylamine also occur in increased amounts in this disease [2].

High impact information on C01888

• Purification and properties of aminoacetone synthetase from beef liver mitochondria [3].
• Methylamine and aminoacetone have been recognized to be physiological substrates for SSAO [4].
• This enzyme catalyzes deamination of methylamine and aminoacetone, leading to production of toxic formaldehyde and methylglyoxal, respectively, as well as hydrogen peroxide and ammonium [5].
• Semicarbazide-sensitive amine oxidase (SSAO) catalyzes the deamination of methylamine and aminoacetone to produce toxic aldehydes, i.e. formaldehyde and methylglyoxal, as well as hydrogen peroxide and ammonia [6].
• Aerobic oxidation of aminoacetone, a threonine catabolite: iron catalysis and coupled iron release from ferritin [7].

Biological context of C01888

• Formaldehyde and methylglyoxal are produced via deamination of, respectively, methylamine and aminoacetone catalyzed by semicarbazide-sensitive amine oxidase (SSAO, EC 1.4.3 [8].
• Oxidative DNA damage induced by aminoacetone, an amino acid metabolite [9].
• It is possible that the increased SSAO activity in diabetes may be a result of up-regulation due to increase of SSAO substrates, such as methylamine or aminoacetone [10].
• The pathway, which involves the two enzymes L-threonine dehydrogenase (EC 1.1.1.103) and aminoacetone synthase (acetyl-CoA:glycine C-acetyltransferase, EC 2.3.1.29) and subsequent hydrolysis of the acetyl-CoA, is most active in cultured trypanosomes but is also present in bloodstream forms [11].

Anatomical context of C01888

• Chicken liver mitochondria contain aminoacetone synthase (acetyl-CoA:glycine C-acetyltransferase (EC 2.3.1.29)) [12].
• Here, aminoacetone is shown to be deaminated to methylglyoxal by supernatants obtained by low speed centrifugation (600 g/10 min) of human umbilical artery homogenates, and also by membrane fractions isolated by high speed centrifugation (105,000 g/60 min) of these supernatants [13].
• Immunostaining of tissue sections showed that aminoacetone-treated rats (normal as well as diabetic) formed more argpyrimidine in aortic smooth muscle than untreated controls [14].
• The formation of 8-oxodG in calf thymus DNA increased due to aminoacetone only in the presence of Cu(II) [9].
• The following article reports (A) data on glyoxalase I activity in skeletal muscle of untrained men and endurance--trained athletes, and (B) the presence at rest and the rise in blood after exercise of two metabolites of the aminoacetone pathway of amino acid degradation in man [15].

Associations of C01888 with other chemical compounds

• TDH activity was determined as aminoacetone and glycine accumulation during incubation of liver mitochondria [16].
• Deamination of aminoacetone was nearly completely inhibited by 1 mM semicarbazide and 1 microM MDL-72974A, a potent selective SSAO inhibitor, whereas MAO inhibitors clorgyline (1 mM) and deprenyl (1 mM) had no inhibitory effect [17].

Gene context of C01888

• Aminoacetone metabolism by semicarbazide-sensitive amine oxidase in rat aorta [18].

Analytical, diagnostic and therapeutic context of C01888

• An HPLC procedure for the determination of SSAO activity toward aminoacetone in vitro is described [17].
• Pulsed-field gel electrophoresis revealed that aminoacetone caused cellular DNA cleavage [9].

References